Molecular Serum Albumin Unmask Nanobio Properties of Molecular Graphenes in Shungite Carbon Nanoparticles

Overview

Journal Int J Mol Sci

Publisher MDPI

Specialties Biochemistry
Chemistry
Molecular Biology

Date 2024 Mar 13

PMID 38473711

Authors

Sergey Rozhkov

Andrey Goryunov

Natalia Rozhkova

Affiliations

Soon will be listed here.

Abstract

Serum albumin is a popular macromolecule for studying the effect of proteins on the colloidal stability of nanoparticle (NP) dispersions, as well as the protein-nanoparticle interaction and protein corona formation. In this work, we analyze the specific conformation-dependent phase, redox, and fatty acid delivery properties of bovine albumin in the presence of shungite carbon (ShC) molecular graphenes stabilized in aqueous dispersions in the form of NPs in order to reveal the features of NP bioactivity. The formation of NP complexes with proteins (protein corona around NP) affects the transport properties of albumin for the delivery of fatty acids. Being acceptors of electrons and ligands, ShC NPs are capable of exhibiting both their own biological activity and significantly affecting conformational and phase transformations in protein systems.

Citing Articles

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Georgieva E, Ananiev J, Yovchev Y, Arabadzhiev G, Abrashev H, Zaharieva V Int J Mol Sci. 2024; 25(15).

PMID: 39125614 PMC: 11312055. DOI: 10.3390/ijms25158045.

References

Yewdall N, Mason A, van Hest J . The hallmarks of living systems: towards creating artificial cells. Interface Focus. 2018; 8(5):20180023. PMC: 6227776. DOI: 10.1098/rsfs.2018.0023. View

Skrypnik L, Babich O, Sukhikh S, Shishko O, Ivanova S, Mozhei O . A Study of the Antioxidant, Cytotoxic Activity and Adsorption Properties of Karelian Shungite by Physicochemical Methods. Antioxidants (Basel). 2021; 10(7). PMC: 8301057. DOI: 10.3390/antiox10071121. View

Jin L, Yu Y, Gao G . A molecular-thermodynamic model for the interactions between globular proteins in aqueous solutions: applications to bovine serum albumin (BSA), lysozyme, alpha-chymotrypsin, and immuno-gamma-globulins (IgG) solutions. J Colloid Interface Sci. 2006; 304(1):77-83. DOI: 10.1016/j.jcis.2006.08.046. View

Andre A, Spruijt E . Liquid-Liquid Phase Separation in Crowded Environments. Int J Mol Sci. 2020; 21(16). PMC: 7460619. DOI: 10.3390/ijms21165908. View

Takabayashi K, Imada T, Saito Y, Inada Y . Coupling between fatty acid binding and sulfhydryl oxidation in bovine serum albumin. Eur J Biochem. 1983; 136(2):291-5. DOI: 10.1111/j.1432-1033.1983.tb07740.x. View

Li D, Zhang W, Yu X, Wang Z, Su Z, Wei G . When biomolecules meet graphene: from molecular level interactions to material design and applications. Nanoscale. 2016; 8(47):19491-19509. DOI: 10.1039/c6nr07249f. View

Nasser F, Constantinou J, Lynch I . Nanomaterials in the Environment Acquire an "Eco-Corona" Impacting their Toxicity to Daphnia Magna-a Call for Updating Toxicity Testing Policies. Proteomics. 2019; 20(9):e1800412. DOI: 10.1002/pmic.201800412. View

Wang Y, Annunziata O . Comparison between protein-polyethylene glycol (PEG) interactions and the effect of PEG on protein-protein interactions using the liquid-liquid phase transition. J Phys Chem B. 2007; 111(5):1222-30. DOI: 10.1021/jp065608u. View

Gryzunov Y, Arroyo A, Vigne J, Zhao Q, Tyurin V, Hubel C . Binding of fatty acids facilitates oxidation of cysteine-34 and converts copper-albumin complexes from antioxidants to prooxidants. Arch Biochem Biophys. 2003; 413(1):53-66. DOI: 10.1016/s0003-9861(03)00091-2. View

10.

Vekilov P . Phase diagrams and kinetics of phase transitions in protein solutions. J Phys Condens Matter. 2012; 24(19):193101. DOI: 10.1088/0953-8984/24/19/193101. View

11.

Cinar H, Fetahaj Z, Cinar S, Vernon R, Chan H, Winter R . Temperature, Hydrostatic Pressure, and Osmolyte Effects on Liquid-Liquid Phase Separation in Protein Condensates: Physical Chemistry and Biological Implications. Chemistry. 2019; 25(57):13049-13069. DOI: 10.1002/chem.201902210. View

12.

Shiryayev A, Pagan D, Gunton J, Rhen D, Saxena A, Lookman T . Role of solvent for globular proteins in solution. J Chem Phys. 2005; 122(23):234911. DOI: 10.1063/1.1931655. View

13.

Sauter A, Roosen-Runge F, Zhang F, Lotze G, Feoktystov A, Jacobs R . On the question of two-step nucleation in protein crystallization. Faraday Discuss. 2015; 179:41-58. DOI: 10.1039/c4fd00225c. View

14.

Kopac T . Protein corona, understanding the nanoparticle-protein interactions and future perspectives: A critical review. Int J Biol Macromol. 2020; 169:290-301. DOI: 10.1016/j.ijbiomac.2020.12.108. View

15.

Lundqvist M, Stigler J, Elia G, Lynch I, Cedervall T, Dawson K . Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc Natl Acad Sci U S A. 2008; 105(38):14265-70. PMC: 2567179. DOI: 10.1073/pnas.0805135105. View

16.

Sheka E . A Neoteric View of Amorphous Carbon. Nanomaterials (Basel). 2023; 13(10). PMC: 10222986. DOI: 10.3390/nano13101648. View

17.

Fullerton G, Kanal K, Cameron I . Osmotically unresponsive water fraction on proteins: non-ideal osmotic pressure of bovine serum albumin as a function of pH and salt concentration. Cell Biol Int. 2005; 30(1):86-92. DOI: 10.1016/j.cellbi.2005.11.001. View

18.

Muravsky V, Gurachevskaya T, Berezenko S, Schnurr K, Gurachevsky A . Fatty acid binding sites of human and bovine albumins: differences observed by spin probe ESR. Spectrochim Acta A Mol Biomol Spectrosc. 2009; 74(1):42-7. DOI: 10.1016/j.saa.2009.05.003. View

19.

Asherie N . Protein crystallization and phase diagrams. Methods. 2004; 34(3):266-72. DOI: 10.1016/j.ymeth.2004.03.028. View

20.

Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K . Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 1999; 12(6):439-46. DOI: 10.1093/protein/12.6.439. View